We have expressed beta-1,4-galactosyltransferase in E. coli as a non fusion protein and regenerated the enzymatic activity of the protein from the inclusion bodies. Currently the protein is being produced in large quantities and methods are being developed (a) to increase the solubility of the protein without any loss of enzymatic activity and (b) perpare high concentrated solution of protein that is desired for crystallization. Furthermore, a number of different methods are being tried simultaneously for the crystallization of the protein with the aim to determine the structure of beta1,4-galactosyltransferase by x- ray crystallographic method.